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上传于：2020-10-08

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本人985学校毕业后一直从事证券类工作，在金融、证券领域有深厚的认识

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    188宝金博页面版: Some comments on John Ferry's most enduring paper(对约翰·费里（John Ferry）最持久的论文的一些评论)

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    内容提示： ARTICLE IN PRESSSome comments on John Ferry’s most enduring paperRussell F. Doolittle *Department of Chemistry and Biochemistry, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093-0634, USAReceived 17 May 2004; accepted 1 July 2004AbstractIn this brief memoir, I reflect on the great insight John Ferry exhibited in his extremely influential 1952 paper on the mechanism offibrinogen being changed into fibrin.D 2004 Elsevier B.V. All rights reserved.Keywords: Fibrinogen; Fibrin; John F...

    文档格式：PDF | 页数：4 | 浏览次数：21 | 上传日期：2020-10-08 02:29:31 | 文档星级：
    ARTICLE IN PRESSSome comments on John Ferry’s most enduring paperRussell F. Doolittle *Department of Chemistry and Biochemistry, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093-0634, USAReceived 17 May 2004; accepted 1 July 2004AbstractIn this brief memoir, I reflect on the great insight John Ferry exhibited in his extremely influential 1952 paper on the mechanism offibrinogen being changed into fibrin.D 2004 Elsevier B.V. All rights reserved.Keywords: Fibrinogen; Fibrin; John Ferry; Physical chemistry of macromolecules1. IntroductionArguably, John Ferry’s most enduring and influentialpaper in the area of fibrinogen–fibrin appeared in July, 1952(a mere 6 weeks after its submission to the Proceedings ofthe National Academy of Science) [1]. It was only fourpages long and contained no illustrations. The heart of thepaper was a simple rendering:Although no new data were presented, the paper was basedon an enormous amount of physicochemical experimenta-tion conducted on fibrinogen and solublized fibrin duringthe previous decade in several laboratories including theFerry lab at the University of Wisconsin.The timely appearance of the paper, however, wasdoubtless tied to a series of biochemical reports that hadappeared in 1950 and 1951. In one of these, Koloman Laki[2] had shown that the action of thrombin could be separatedfrom the polymerization phase in that fibrinogen treatedwith thrombin at pH 5 did not clot, but upon neutralizationto pH 7 instantaneously gelled. In another key experiment,Elemer Mihalyi [3] had shown that fibrinogen and fibrindissolved in urea solutions had measurably different iso-electric points, fibrinogen having more negative charge atneutral pH than fibrin under the same conditions. Finally, itwas found by both Kenneth Bailey and Lazlo Lorand andtheir respective colleagues that thrombin effected a changein the amino-terminal groups of fibrinogen and fibrin [4].Taken in aggregate, these studies showed that thrombinremoved one or more negatively charged groups from thestarting fibrinogen molecule. That proteolysis might beinvolved in the bactivationQ of fibrinogen had long beensuspected.The demonstration of limited proteolysis provided thelast key in a general understanding of how the solubleprotein fibrinogen is transformed into the insoluble poly-meric gel called fibrin, capping the tremendous amount ofphysicochemical experimentation that had already beenperformed on fibrinogen and fibrin in different solutionenvironments.In the 1952 paper, John Ferry laid it all out clearly andsimply. Thrombin modified the fibrinogen in such a way, heconjectured, that it exposed a region of positive charge onthe sides of an elongated molecule, leading to intermolec-ular associations with negatively charged regions near theends of neighboring molecules in a kind of staggeredoverlap. The intermediate polymer grew progressively bythe same process until it reached a critical length, after0301-4622/$ - see front matter D 2004 Elsevier B.V. All rights reserved.doi:10.1016/j.bpc.2004.07.045* Tel.: +1 858 534 4417; fax: +1 858 534 4985.E-mail address: rdoolittle@ucsd.edu.Biophysical Chemistry xx (2004) xxx–xxxwww.elsevier.com/locate/bpcBIOCHE-04447; No of Pages 4DTD 5

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